Evidence map›Paper›PMID 38258382›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2024

Membrane Condensation and Curvature Induced by SARS-CoV-2 Envelope Protein.

Christian Wölk, Chen Shen, Gerd Hause, Wahyu Surya, Jaume Torres, Richard D Harvey, Gianluca Bello

Open access · hybridAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. SARS-CoV-2 Viroporin E Induces CaInternational journal of molecular sciences · 2024
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 3 countries.

Christian WölkPharmaceutical Technology, Medical Faculty, University Leipzig, Eilenburger Straße 15a, 04317 Leipzig, Germany.ORCID 0000-0002-8067-7307
Chen ShenDeutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.ORCID 0000-0002-7855-1764
Gerd HauseBiocenter, Martin-Luther University Halle-Wittenberg, Weinbergweg 22, 06120 Halle (Saale), Germany.
Wahyu SuryaSchool of Biological Sciences, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.ORCID 0000-0001-9240-371X
Jaume TorresSchool of Biological Sciences, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.
Richard D HarveyDivision of Pharmaceutical Chemistry, Department of Pharmaceutical Sciences, University of Vienna, Josef-Holaubek-Platz 2, UZA 2, Vienna 1090, Austria.ORCID 0000-0003-3625-4654
Gianluca BelloDivision of Pharmaceutical Chemistry, Department of Pharmaceutical Sciences, University of Vienna, Josef-Holaubek-Platz 2, UZA 2, Vienna 1090, Austria.
Nanyang Technological University · SGUniversity of Vienna · ATDeutsches Elektronen-Synchrotron DESY · DEMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The envelope (E) protein of SARS-CoV-2 participates in virion encapsulation and budding at the membrane of the endoplasmic reticulum Golgi intermediate compartment (ERGIC). The positively curved membrane topology required to fit an 80 nm viral particle is energetically unfavorable; therefore, viral proteins must facilitate ERGIC membrane curvature alteration. To study the possible role of the E protein in this mechanism, we examined the structural modification of the host lipid membrane by the SARS-CoV-2 E protein using synchrotron-based X-ray methods. Our reflectometry results on solid-supported planar bilayers show that E protein markedly condenses the surrounding lipid bilayer. For vesicles, this condensation effect differs between the two leaflets such that the membrane becomes asymmetric and increases its curvature. The formation of such a curved and condensed membrane is consistent with the requirements to stably encapsulate a viral core and supports a role for E protein in budding during SARS-CoV-2 virion assembly.

Indexed as

COVID-19SARS-CoV-2HumansViral Envelope ProteinsViral ProteinsVirus AssemblyViral Envelope ProteinsViral Proteins

Identifiers

PMID38258382
PMCPMC10851660
OpenAlexW4391141568

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.